Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13.

The ubiquitin conjugating enzyme complex Mms2-Ubc13 plays a key role in post-replicative DNA repair in yeast and the NF-kappaB signal transduction pathway in humans. This complex assembles novel polyubiquitin chains onto yet uncharacterized protein targets. Here we report the crystal structure of a complex between hMms2 (Uev1) and hUbc13 at ...
1.85 A resolution and a structure of free hMms2 at 1.9 A resolution. These structures reveal that the hMms2 monomer undergoes a localized conformational change upon interaction with hUbc13. The nature of the interface provides a physical basis for the preference of Mms2 for Ubc13 as a partner over a variety of other structurally similar ubiquitin-conjugating enzymes. The structure of the hMms2-hUbc13 complex provides the conceptual foundation for understanding the mechanism of Lys 63 multiubiquitin chain assembly and for its interactions with the RING finger proteins Rad5 and Traf6.
Mesh Terms:
Adenosine Triphosphatases, Amino Acid Motifs, Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, DNA Helicases, Fungal Proteins, Humans, Ligases, Macromolecular Substances, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Structure, Secondary, Proteins, Saccharomyces cerevisiae Proteins, Sequence Alignment, Structure-Activity Relationship, Substrate Specificity, TNF Receptor-Associated Factor 6, Trans-Activators, Ubiquitin-Conjugating Enzymes, Ubiquitins
Nat. Struct. Biol.
Date: Aug. 01, 2001
Download Curated Data For This Publication
55241
Switch View:
  • Interactions 1